Összes fotó(6)
Fontos dokumentumok
G4387
L-Glutamic Dehydrogenase (NADP) from Proteus sp.
buffered aqueous solution, ≥4,000 units/mL
Szinonimák:
L-Glutamate:NADP+ oxidoreductase (deaminating)
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(6)
About This Item
CAS-szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54
Javasolt termékek
biológiai forrás
bacterial (Proteus spp.)
Minőségi szint
Forma
buffered aqueous solution
specifikus aktivitás
≥4,000 units/mL
molekulatömeg
~300 kDa
tárolási hőmérséklet
2-8°C
Alkalmazás
This enzyme is useful for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201) in clinical analysis. In vitro, various activity assays of this enzyme examine the conversion of α-ketoglutarate to L-glutamate, in the presence of excess ammonium ions (NH4+) and NADPH.
Biokémiai/fiziológiai hatások
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
Fizikai tulajdonságok
Isoelectric point : 4.6
Michaelis constants : 1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate)
1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+)
Structure : 6 subunits (M.W.50,000) per mol of enzyme
Inhibitors : Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine,
2,2′-dithiopyridine
Optimum pH : 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature : 45oC(α-KG−L-Glu) 45-55oC (L-Glu→α-KG)
pH stability : pH 6.0 - 8.5 (25oC, 20hr)
Thermal stability : below 50oC (pH 7.4, 10min)
Michaelis constants : 1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate)
1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+)
Structure : 6 subunits (M.W.50,000) per mol of enzyme
Inhibitors : Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine,
2,2′-dithiopyridine
Optimum pH : 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature : 45oC(α-KG−L-Glu) 45-55oC (L-Glu→α-KG)
pH stability : pH 6.0 - 8.5 (25oC, 20hr)
Thermal stability : below 50oC (pH 7.4, 10min)
Egység definíció
One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30 °C in the presence of ammonium ions and NADPH.
Fizikai forma
Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide
Egyéb megjegyzések
Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.
Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 3
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Analitikai tanúsítványok (COA)
Lot/Batch Number
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Az ügyfelek ezeket is megtekintették
J Bailey et al.
The Journal of biological chemistry, 257(10), 5579-5583 (1982-05-25)
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At ph 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both
Daria V Borsakova et al.
Scientific reports, 12(1), 5437-5437 (2022-04-02)
Excessive ammonium blood concentration causes many serious neurological complications. The medications currently used are not very effective. To remove ammonium from the blood, erythrocyte-bioreactors containing enzymes that processing ammonium have been proposed. The most promising bioreactor contained co-encapsulated glutamate dehydrogenase
D P Hornby et al.
The Biochemical journal, 223(1), 161-168 (1984-10-01)
In steady-state kinetic studies of ox liver glutamate dehydrogenase in 0.11 M-potassium phosphate buffer, pH7, at 25 degrees C, the concentration of ADP was varied from 0.5 to 1000 microM. Inhibition was observed except when the concentrations of both glutamate
Wei-Li Liao et al.
Fungal genetics and biology : FG & B, 45(4), 514-526 (2007-10-24)
The function of GLN3, a GATA factor encoding gene, in nitrogen metabolism of Candida albicans was examined. GLN3 null mutants had reduced growth rates on multiple nitrogen sources. More severe growth defects were observed in mutants lacking both GLN3 and
S Cossy Isasi et al.
Experimental parasitology, 122(3), 218-225 (2009-04-09)
Biochemical and structural modifications were investigated in axenic cultured Trypanosoma cruzi after treatment with gangliosides. Fluorescence anisotropy showed dose dependent increments in parasite membranes of ganglioside treated epimastigotes. NADP-GDH activity increased in parasites treated at day 4 (13%), 7 (137.2%)
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